ID A0A2U2HPM3_9BURK Unreviewed; 343 AA.
AC A0A2U2HPM3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:PWF49385.1};
GN ORFNames=C7C56_006915 {ECO:0000313|EMBL:PWF49385.1};
OS Massilia glaciei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF49385.1, ECO:0000313|Proteomes:UP000241421};
RN [1] {ECO:0000313|EMBL:PWF49385.1, ECO:0000313|Proteomes:UP000241421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B448-2 {ECO:0000313|EMBL:PWF49385.1,
RC ECO:0000313|Proteomes:UP000241421};
RA Wang H.;
RT "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang, China.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWF49385.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXWF02000092; PWF49385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2HPM3; -.
DR OrthoDB; 9787225at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000241421; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582:SF30; BLR4375 PROTEIN; 1.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000241421};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..120
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 210..339
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 35249 MW; 59A4FCF27360CEDC CRC64;
MAQPPAAAPA PGDTAATTAA TAATTTTTTS TTPKAAKNAK AAVTLDAATV NAPGAPAVAP
ARADAASVLR AQILLNRARF SSGEIDAAFG SNVRQALSGY QRKMGLPATG VADAATWAAL
NAGAAAALVT YTITDADVAG PFVAIPQKMA DKAKLSALGY SSVEEALGEK FHASPALLQR
LNPGKNFSRA GEQIIVPNVL DTEPLPKASQ IVVDKTDRTL TLMDGDGKPM AQFPVTTGSK
HDPLPLGKWK VNGISKAPVF HYNPALFWDA TAGDKKAKIP AGPNNPVGVA WVDLSKPHYG
IHGTPVPASI GKTESHGCIR MTNWDVTTMM QSVGSGTAVL LKE
//